메뉴 건너뛰기




Volumn 61, Issue 5-6, 2003, Pages 463-471

Purification, characterization, and molecular cloning of a novel amine:pyruvate transaminase from Vibrio fluvialis JS17

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA METHYLBENZYLAMINE; AMINE:PYRUVATE TRANSAMINASE; AMINOTRANSFERASE; OMEGA AMINO ACID; PYRIDOXAL 5 PHOSPHATE; PYRUVIC ACID; UNCLASSIFIED DRUG;

EID: 0038236890     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-003-1250-6     Document Type: Article
Times cited : (143)

References (28)
  • 1
    • 0029782672 scopus 로고    scopus 로고
    • Stereospecific production of the herbicide phosphinothricin: Purification of aspartate transaminase from Bacillus stearothermophilus, cloning of the corresponding gene, aspC, and application in a coupled transaminase process
    • Bartsch K, Schneider R, Schulz A (1996) Stereospecific production of the herbicide phosphinothricin: purification of aspartate transaminase from Bacillus stearothermophilus, cloning of the corresponding gene, aspC, and application in a coupled transaminase process. Appl Environ Microbiol 62:3794-3799
    • (1996) Appl Environ Microbiol , vol.62 , pp. 3794-3799
    • Bartsch, K.1    Schneider, R.2    Schulz, A.3
  • 2
    • 0026645203 scopus 로고
    • Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp.
    • Bierman J, Logan R, O'Brien K, Seno ET, Rao RN, Schoner BE (1992) Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp. Gene 116:43-49
    • (1992) Gene , vol.116 , pp. 43-49
    • Bierman, J.1    Logan, R.2    O'Brien, K.3    Seno, E.T.4    Rao, R.N.5    Schoner, B.E.6
  • 3
    • 0344258317 scopus 로고    scopus 로고
    • Enhanced conversion rate of L-phenylalanine by coupling reactions of aminotransferases and phosphoenolpyruvate carboxykinase in Escherichia coli K-12
    • Chao Y-P, Lai ZJ, Chen P, Chern J-T (1999) Enhanced conversion rate of L-phenylalanine by coupling reactions of aminotransferases and phosphoenolpyruvate carboxykinase in Escherichia coli K-12. Biotechnol Prog 15:453-458
    • (1999) Biotechnol Prog , vol.15 , pp. 453-458
    • Chao, Y.-P.1    Lai, Z.J.2    Chen, P.3    Chern, J.-T.4
  • 6
    • 0018496454 scopus 로고
    • High performance liquid chromatographic determination of amino acids in the picomole range
    • Dennis WH, Walters FH, Wilson TD, Stuart JD (1979) High performance liquid chromatographic determination of amino acids in the picomole range. Anal Chem 51:391-395
    • (1979) Anal Chem , vol.51 , pp. 391-395
    • Dennis, W.H.1    Walters, F.H.2    Wilson, T.D.3    Stuart, J.D.4
  • 7
    • 0024234855 scopus 로고
    • CLUSTAL: A package for performing multiple sequence alignment on a microcomputer
    • Higgins DG, Sharp PM (1988) CLUSTAL: a package for performing multiple sequence alignment on a microcomputer. Gene 73:237-244
    • (1988) Gene , vol.73 , pp. 237-244
    • Higgins, D.G.1    Sharp, P.M.2
  • 9
    • 0032478092 scopus 로고    scopus 로고
    • Substrate inhibition of D-amino acid transaminase and protection by salts and by reduced nicotinamide adenine dinucleotide: Isolation and initial characterization of a pyridoxo intermediate related to inactivation
    • Manning JM (1998) Substrate inhibition of D-amino acid transaminase and protection by salts and by reduced nicotinamide adenine dinucleotide: isolation and initial characterization of a pyridoxo intermediate related to inactivation. Biochemistry 37:2879-2888
    • (1998) Biochemistry , vol.37 , pp. 2879-2888
    • Manning, J.M.1
  • 10
    • 0028358526 scopus 로고
    • Homology of 1-aminocyclopropane-1-carboxylate synthase, D-amino-7-oxononanoate synthase, 2-amino-6-carprolactam racemase, 2,2-dialkylglycine decarboxylase, glutamate-1-semialdehyde 1,2-aminomutase and isopenicillin-N-epimerase with aminotransferases
    • Mehta PK, Christen P (1994) Homology of 1-aminocyclopropane-1-carboxylate synthase, D-amino-7-oxononanoate synthase, 2-amino-6-carprolactam racemase, 2,2-dialkylglycine decarboxylase, glutamate-1-semialdehyde 1,2-aminomutase and isopenicillin-N-epimerase with aminotransferases. Biochem Biophys Res Commun 198:138-143
    • (1994) Biochem Biophys Res Commun , vol.198 , pp. 138-143
    • Mehta, P.K.1    Christen, P.2
  • 11
    • 0027297771 scopus 로고
    • Aminotransferases: Demonstration of homology and division into evolutionary subgroups
    • Mehta PK, Hale TI, Christen P (1993) Aminotransferases: demonstration of homology and division into evolutionary subgroups. Eur J Biochem 214:549-569
    • (1993) Eur J Biochem , vol.214 , pp. 549-569
    • Mehta, P.K.1    Hale, T.I.2    Christen, P.3
  • 15
    • 0343907783 scopus 로고    scopus 로고
    • Kinetic resolution of α-methylbenzylamine with ω-transaminase screened from soil microorganisms: Application of a biphasic system to overcome product inhibition
    • Shin J-S, Kim B-G (1997) Kinetic resolution of α-methylbenzylamine with ω-transaminase screened from soil microorganisms: application of a biphasic system to overcome product inhibition. Biotechnol Bioeng 55:348-358
    • (1997) Biotechnol Bioeng , vol.55 , pp. 348-358
    • Shin, J.-S.1    Kim, B.-G.2
  • 16
    • 0032488279 scopus 로고    scopus 로고
    • Kinetic modeling of ω-transamination for enzymatic kinetic resolution of α-methylbenzylamine
    • Shin J-S, Kim B-G (1998) Kinetic modeling of ω-transamination for enzymatic kinetic resolution of α-methylbenzylamine. Biotechnol Bioeng 60:534-540
    • (1998) Biotechnol Bioeng , vol.60 , pp. 534-540
    • Shin, J.-S.1    Kim, B.-G.2
  • 17
    • 0033589366 scopus 로고    scopus 로고
    • Asymmetric synthesis of chiral amines with ω-transaminase
    • Shin J-S, Kim B-G (1999) Asymmetric synthesis of chiral amines with ω-transaminase. Biotechnol Bioeng 65:206-211
    • (1999) Biotechnol Bioeng , vol.65 , pp. 206-211
    • Shin, J.-S.1    Kim, B.-G.2
  • 18
    • 0035433593 scopus 로고    scopus 로고
    • Comparison of the ω-transaminases from different microorganisms and application to production of chiral amines
    • Shin J-S, Kim B-G (2001) Comparison of the ω-transaminases from different microorganisms and application to production of chiral amines. Biosci Biotechnol Biochem 65:1782-1788
    • (2001) Biosci Biotechnol Biochem , vol.65 , pp. 1782-1788
    • Shin, J.-S.1    Kim, B.-G.2
  • 19
    • 0035810702 scopus 로고    scopus 로고
    • Kinetic resolution of chiral amines using enzyme-membrane reactor
    • Shin J-S, Kim B-G, Liese A, Wandrey C (2001) Kinetic resolution of chiral amines using enzyme-membrane reactor. Biotechnol Bioeng 73:179-187
    • (2001) Biotechnol Bioeng , vol.73 , pp. 179-187
    • Shin, J.-S.1    Kim, B.-G.2    Liese, A.3    Wandrey, C.4
  • 20
    • 84885111751 scopus 로고    scopus 로고
    • Chiral drug market shows signs of maturity
    • Stinson SC (1997) Chiral drug market shows signs of maturity. Chem Eng News October 20:38-70
    • (1997) Chem Eng News October , vol.20 , pp. 38-70
    • Stinson, S.C.1
  • 21
    • 0000980630 scopus 로고
    • The use of aminotransferases for the production of chiral amino acids and amines
    • Collins AN, Sheldrake GN, Crosby J (eds). Wiley, New York
    • Stirling DI (1992) The use of aminotransferases for the production of chiral amino acids and amines. In: Collins AN, Sheldrake GN, Crosby J (eds) Chirality in industry. Wiley, New York, p 209
    • (1992) Chirality in Industry , pp. 209
    • Stirling, D.I.1
  • 23
    • 0031731648 scopus 로고    scopus 로고
    • Novel biosynthetic approaches to the production of unnatural amino acids using transaminases
    • Taylor PP, Pantaleone DP, Senkpeil RF, Fotheringham IG (1998) Novel biosynthetic approaches to the production of unnatural amino acids using transaminases. Trends Biotechnol 16:412-418
    • (1998) Trends Biotechnol , vol.16 , pp. 412-418
    • Taylor, P.P.1    Pantaleone, D.P.2    Senkpeil, R.F.3    Fotheringham, I.G.4
  • 24
    • 0018885263 scopus 로고
    • Aminobutyrate: α-ketoglutarate aminotransferase from Pseudomonas sp. F-126: Purification, crystallization, and enzymologic properties
    • Yonaha K, Yonaha S (1980) Aminobutyrate: α-ketoglutarate aminotransferase from Pseudomonas sp. F-126: purification, crystallization, and enzymologic properties. Arch Biochem Biophys 200:156-164
    • (1980) Arch Biochem Biophys , vol.200 , pp. 156-164
    • Yonaha, K.1    Yonaha, S.2
  • 25
    • 0011856409 scopus 로고
    • Distribution of ω-amino acid: Pyruvate transferase and aminobutyrate: α-ketoglutarate transaminase in microorganisms
    • Yonaha K, Suzuki K, Minei H, Toyama S (1983a) Distribution of ω-amino acid: pyruvate transferase and aminobutyrate: α-ketoglutarate transaminase in microorganisms. Agric Biol Chem 47:2257-2265
    • (1983) Agric Biol Chem , vol.47 , pp. 2257-2265
    • Yonaha, K.1    Suzuki, K.2    Minei, H.3    Toyama, S.4
  • 26
    • 0021111654 scopus 로고
    • Properties of the bound coenzyme and subunit structure of ω-amino acid:pyruvate aminotransferase
    • Yonaha K, Toyama S, Kagamiyama H (1983b) Properties of the bound coenzyme and subunit structure of ω-amino acid:pyruvate aminotransferase. J Biol Chem 258:2260-2265
    • (1983) J Biol Chem , vol.258 , pp. 2260-2265
    • Yonaha, K.1    Toyama, S.2    Kagamiyama, H.3
  • 27
    • 0023088228 scopus 로고
    • ω-Amino acid-pyruvate aminotransferase
    • Yonaha K, Toyama S, Soda K (1987) ω-Amino acid-pyruvate aminotransferase. Methods Enzymol 143:500-505
    • (1987) Methods Enzymol , vol.143 , pp. 500-505
    • Yonaha, K.1    Toyama, S.2    Soda, K.3
  • 28
    • 0026747089 scopus 로고
    • The primary structure of omega-amino acid:pyruvate aminotransferase
    • Yonaha K, Nishie M, Aibara S (1992) The primary structure of omega-amino acid:pyruvate aminotransferase. J Biol Chem 267:12506-12510
    • (1992) J Biol Chem , vol.267 , pp. 12506-12510
    • Yonaha, K.1    Nishie, M.2    Aibara, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.